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1lv4

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Revision as of 03:52, 11 September 2015

Human catestatin 21-mer

Structural highlights

1lv4 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1cfk, 1krk
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CMGA_HUMAN] Pancreastatin strongly inhibits glucose induced insulin release from the pancreas.

Publication Abstract from PubMed

Previous modeling (PDB 1cfk) of the catecholamine release-inhibitory "catestatin" region of chromogranin A (CgA) suggested a beta-strand/loop/beta-strand active conformation, displaying an electropositive Arg-rich loop (R(351)AR(353)GYGFR(358)). To explore this possibility, we studied NMR structures of linear and cyclic synthetic catestatin, bovine (bCgA(344-364)) or human (hCgA(352-372)). By 2-D (1)H-NMR, the structure of linear catestatin (hCgA(352-372)) exhibited the NOE pattern of a coiled loop (PDB 1lv4). We then constrained the structure, cyclizing the putative Arg-rich loop connecting the beta-strands: cyclic bCgA(350-362) ([C(0)]F(350)RARGYGFRGPGL(362)[C(+14)]). Favored conformations of cyclic bCgA(350-362) were determined by (1)H-NMR and (13)C-NMR spectroscopy. Cyclic bCgA(350-362) conformers (PDB 1n2y) adopted a "twisted-loop" conformation. Alignment between the homology model and the cyclic NMR structure showed that, while portions of the NMR structure's mid-molecule and carboxy-terminus were congruent with the homology model (RMSD, 1.61-1.91 A), the amino-terminal "twisted loop" coiled inward and away from the model (RMSD, 3.36 A). Constrained cyclic bCgA(350-362) did not exert nicotinic cholinergic antagonist activity (IC(50)>10 microM), when compared to full-length linear (IC(50) approximately 0.42-0.56 microM), or cyclic (IC(50) approximately 0.74 microM) catestatin. Thus, loss of activity in the small, constrained peptide did not result from either [Cys]-extension or cyclization, per se. While linear catestatin displays coiled character, a small cyclic derivative lost biological activity, perhaps because its amino-terminal domain deviated sharply from the predicted active conformation. These results refine the relationship between structure and function in catestatin, and suggest goals in future peptidomimetic syntheses, in particular attempts to constrain the correct amino-terminal shape for biological activity.

Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A.,Preece NE, Nguyen M, Mahata M, Mahata SK, Mahapatra NR, Tsigelny I, O'Connor DT Regul Pept. 2004 Apr 15;118(1-2):75-87. PMID:14759560^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Preece NE, Nguyen M, Mahata M, Mahata SK, Mahapatra NR, Tsigelny I, O'Connor DT. Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A. Regul Pept. 2004 Apr 15;118(1-2):75-87. PMID:14759560 doi:http://dx.doi.org/10.1016/j.regpep.2003.10.035

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lv4"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1lv4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LV4 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cfk|1cfk]], [[1krk|1krk]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lv4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1lv4 RCSB], [http://www.ebi.ac.uk/pdbsum/1lv4 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lv4 OCA], [http://pdbe.org/1lv4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lv4 RCSB], [http://www.ebi.ac.uk/pdbsum/1lv4 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1lv4" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1lv4

From Proteopedia

Revision as of 03:52, 11 September 2015

Human catestatin 21-mer

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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